期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1990
卷号：87
期号：7
页码：2638-2642
DOI：10.1073/pnas.87.7.2638
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：An antiserum specific for P47gag-crk, the oncogene product of avian sarcoma virus CT10, was used to investigate possible crk-binding proteins. In in vitro kinase assays, four proteins were phosphorylated in anti-crk immunoprecipitates. Tyrosine, serine, and threonine residues were phosphorylated. A number of tyrosine-phosphorylated proteins were identified in anti-crk immunoprecipitates of 32P-labeled cells, including the three major phosphotyrosine-containing proteins of CT10-infected cells. These three proteins also bound to bacterially synthesized crk protein. These results suggest that the crk transforming protein can stably associate with both endogenous kinases and cellular kinase substrates.
